PDBsum entry 1jdk

Viral protein

PDB id: 1jdk

Contents

Protein chain

14 a.a.

PDB id:

1jdk

Name:

Viral protein

Title:

Solution structure of lactam analogue (edap) of HIV gp41 600-612 loop.

Structure:

Acetyl group. Chain: a. Engineered: yes

Source:

Synthetic: yes. Other_details: the parent peptide iwgcsgklictta occurs naturally in HIV gp41 glycoprotein

NMR struc:

25 models

Authors:

A.Phan Chan Du,D.Limal,V.Semetey,H.Dali,M.Jolivet,C.Desgranges, M.T.Cung,J.P.Briand,M.C.Petit,S.Muller

Key ref:

A.P.Du et al. (2002). Structural and immunological characterisation of heteroclitic peptide analogues corresponding to the 600-612 region of the HIV envelope gp41 glycoprotein. J Mol Biol, 323, 503-521. PubMed id: 12381305 DOI: 10.1016/S0022-2836(02)00701-5

Date:

14-Jun-01 Release date: 01-Jul-03

Protein chain

No UniProt id for this chain

Struc: 13 a.a.

DOI no: 10.1016/S0022-2836(02)00701-5

J Mol Biol 323:503-521 (2002)

PubMed id: 12381305

Structural and immunological characterisation of heteroclitic peptide analogues corresponding to the 600-612 region of the HIV envelope gp41 glycoprotein.

A.P.Du, D.Limal, V.Semetey, H.Dali, M.Jolivet, C.Desgranges, M.T.Cung, J.P.Briand, M.C.Petit, S.Muller.

ABSTRACT

The conformational and immunological properties of different analogues corresponding to the 600-612 disulfide loop of the human immunodeficiency virus (HIV) gp41 glycoprotein envelope were studied. Fourteen analogues were designed and synthesised; namely, a series of seven analogues in which the disulfide bond was replaced by a lactam bridge and a series of seven analogues in which one residue of each analogue at a time, was replaced by its corresponding homologised alpha-amino acid (beta(3)-amino acid). In the case of the lactam analogues, the influence of the two possible CO-NH and NH-CO orientations of the lactam bridge as well as the size of the lactam ring was explored. The analogues were tested in ELISA with monoclonal antibodies raised against the 600-612 cyclic parent peptide as well as with sera from HIV-1 infected patients. A structural analysis of the parent and analogue peptides was carried out in dimethyl sulfoxide (DMSO-d(6)) using two-dimensional NMR techniques and molecular dynamics simulations. Comparison of the own conformation of the cyclic analogues with their either strong or weak reactivity with the antibodies reveals structural features that may be correlated with the antibody reactivity. Thus, a close structural similarity, particularly a characteristic orientation of the side-chains of residues Lys606, Leu607 and Ile608 in the loop, was found in certain beta(3)-analogues that were better recognised than the parent peptide by anti-peptide mouse monoclonal antibodies and patients' antibodies.

Selected figure(s)

The above figure is reprinted by permission from Elsevier: J Mol Biol (2002, 323, 503-521) copyright 2002.

Figure was selected by an automated process.